Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum lysozyme has been demonstrated to be an indicator for macrophage activity in the tumor-bearing host. Therefore, we investigated lysozyme levels in the sera of 336 untreated tumor patients (121 malignant melanoma, 61 lung cancers, 70 cervical cancers, 49 breast cancers and 35 benign breast tumors, and 36 healthy controls). Patients with malignant melanoma and lung cancer had significantly higher lysozyme levels than the healthy controls. Within the clinical stages in melanoma, there was a decrease of lysozyme in stages II and III in comparison to stage I, but still above that of the control values. Patients with benign breast tumors had normal levels, whereas in breast cancer patients of stages I and II there was a significant reduction in the lysozyme levels. In stages III and IV no differences to the control group could be detected. In patients with cervical cancer (FIGO II and III) serum lysozyme levels were found to be within the normal range. From this study it can not be concluded that serum lysozyme reflects the immunological reactivity of the tumor bearer. Nevertheless, the reduced levels in stages I and II of breast cancer might point to an immunological defect.
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PMID:Serum lysozyme levels in patients with solid tumors. 45 Mar 87

Serum lysozyme activity was measured in groups of untreated patients with malignant melanoma, hyperneophroma and breast carcinoma. Significant elevation of serum levels of the enzyme was confined to patients with localized disease. In the presence of metastatic disease such elevation was not detected. The rise in serum lysozyme activity was not due to renal damage or any infective process and in the case of malignant melanoma was shown to be associated with infiltration of the tumour mass by macrophages. In vitro studies demonstrated that the macrophages resident in a tumour mass are responsible for relasing lysozyme in large amounts. It is proposed that the elevation of serum lysozyme in these cases may be an indicator of macrophage-mediated host resistance and that the measurement of macrophage products such as lysozyme in the extracellular fluid may under well defined conditions provide useful clinical information concerning host reactions.
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PMID:Serum lysozyme as a marker of host resistance. II. Patients with malignant melanoma, hypernephroma or breast carcinoma. 93 9

Using the avidin-biotin complex immunoperoxidase technique and antibodies to myoglobin, desmin, CLA, NSE, GFAP, keratin, fibronectin, alpha 1AT, lysozyme, S-100 protein, vimentin, cytokeratin, actin, the authors studied 60 cases of rhabdomyosarcoma (RMS) histopathologically diagnosed previously. Thirty-six cases showed both myoglobin and desmin positive stain, an objective evidence of the origin from skeletal muscles. The other 24 cases were identified as of non-skeletal muscle origin, including MFH, lymphoma, melanoma, neuroblastoma, malignant neurilemmoma, leiomyosarcoma etc. This study strongly suggests that histologic examination of RMS may lead to incorrect diagnosis. Histologically MFH and other types of spindle cell sarcomas invading normal skeletal muscles may be confused with pleomorphic RMS, lymphoma and neuroblastoma may be confused with embryonic RMS. Our findings indicate that myoglobin is a highly sensitive and specific tumor marker for RMS.
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PMID:[Immunohistochemical differential diagnosis of 60 cases of rhabdomyosarcoma]. 166 97

The oral administration of hen egg-white lysozyme to mice bearing B16 melanoma significantly reduces the formation of spontaneous lung metastases and, when combined with surgical removal of the primary tumor, prolongs the survival of the treated hosts. The antimetastatic effect, comparable with that found in the Lewis lung carcinoma and MCa mammary carcinoma systems, is independent of the direct interaction of lysozyme with tumor cells and tends to indicate the suggested intervention of an indirect action mediated by the induction of host responses.
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PMID:Reduction of B16 melanoma metastases by oral administration of egg-white lysozyme. 259 13

Malignant fibrous histiocytomas (MFH) belong to the most frequent soft tissue tumours in adults and have to be discriminated from other tumours with similar morphology. Various tumour markers aid the differential diagnosis. Twenty cases of MFH were studied immunohistochemically using antibodies to vimentin, TPA, desmin, lysozyme, alpha 1-antitrypsin, alpha 1-antichymotrypsin, S-100 protein, neurone-specific enolase (NSE), laminin, fibronectin and ferritin. Vimentin and lysozyme were found in the tumour cells of all, alpha 1-antitrypsin of 18, alpha 1-antichymotrypsin of 19, fibronectin of 16 and ferritin of 12 cases. Antibodies of TPA, desmin, S-100 protein, NSE and laminin did not reveal positive immunoreactivity. Exclusion of spindle-cell carcinoma can be made by positive vimentin and negative TPA reactivity, of melanoma by negative S-100 reactivity, and of leio- and rhabdomyosarcoma by lack of desmin immunoreactivity. Schwannomas contain S-100 protein, but lack lysozyme, alpha 1-antitrypsin, alpha 1-antichymotrypsin and fibronectin. Pleomorphic liposarcomas cannot be distinguished from MFH on the basis of immunohistochemical staining. Vimentin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and fibronectin can, therefore, be regarded as useful markers in the differential diagnosis of MFH.
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PMID:[Immunohistochemical studies in the differential diagnosis of malignant fibrous histiocytoma]. 302 16

We used immunohistochemistry to evaluate four cytologically malignant cutaneous neoplasms on the face or neck of elderly individuals. All four lesions were composed of a dermal proliferation of spindle and pleomorphic giant cells. Differential diagnosis included spindle cell carcinoma, atypical fibroxanthoma, malignant melanoma, leiomyosarcoma, and angiosarcoma. All four neoplasms were strongly immunoreactive for vimentin and negative for cytokeratin, S100 protein, desmin, and factor-VIII-related antigen. Focal immunoreactivity for lysozyme and/or a1-antichymotrypsin was seen in the giant cells of each lesion. These results supported the diagnosis of atypical fibroxanthoma in each instance. Immunohistochemical staining can provide useful information for distinguishing among malignant cutaneous spindle cell tumors.
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PMID:Immunohistochemistry: a useful adjunct in the evaluation of malignant cutaneous spindle cell tumors. 320 Dec 97

A case of recurrent Hodgkin's disease of the "sarcomatoid" or "syncytial variant" type was seen that occurred as an extension from the mediastinum to a previously uninvolved extranodal site (breast) and pericardium after treatment of classical nodular sclerosing Hodgkin's disease based in the lymph nodes. This histologic variant was composed of sheets of large, undifferentiated neoplastic cells with few, if any, diagnostic features of nodular sclerosing Hodgkin's disease. For this reason, the differential diagnosis of this variant was difficult and included non-Hodgkin's lymphoma (peripheral T-cell lymphoma), Ki-1-positive lymphoma, medullary carcinoma, metastatic carcinoma, melanoma, and granulocytic sarcoma. Immunologic analysis by immunoperoxidase technique showed a phenotype consistent with "syncytial variant" Hodgkin's disease: Leu-M1+, Ki-1+, IL-2+, HLA-DR+, T11-, pan B-, K-, lambda-, cytokeratin-, S-100-, muramidase-.
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PMID:Recurrent "syncytial variant" of Hodgkin's disease: an immunohistologic diagnosis. 359 90

A murine monoclonal antibody, VM-1, which binds to basal cells of normal human epidermis, reduces the ability of human squamous cell carcinoma cells (SCL-1) derived from the skin to attach and spread on collagen by about 50% and causes cell rounding. Similar effects have been previously shown using normal human keratinocytes. The attachment of cell lines derived from human lung squamous cell carcinomas (SW1271 and SW900), melanoma A375, glioblastoma 126, and fibrosarcoma HT1080 is also inhibited by this antibody. VM-1 antibody does not bind to normal human fibroblasts, benign nevus cells, or the human B-cell-derived line 8866. VM-1 antibody inhibits the growth of SCL-1 cells in vitro as measured by cell numbers and [3H]thymidine ([3H]TdR) incorporation. It is not cytolytic in the presence of complement as measured by 51Cr release. Repeated treatment of SCL-1 cells with VM-1 antibody significantly reduces the proportion of SCL-1 cells that attach to collagen. In addition, after treatment of SCL-1 cells with VM-1 antibody, several proteins can no longer be demonstrated by gel electrophoresis of the cell-free supernatant. The VM-1 antibody effect on attachment and spreading is partially reversed by pretreatment of the collagen surface with laminin and fibronectin, but not with the carbohydrates chondroitin-6-sulfate or hyaluronic acid or with the protein lysozyme. By fluorescence staining, the antigen recognized by VM-1 antibody is membrane-bound and Triton X-100 extractable. The VM-1 antigen is excluded from Bio-Sil TSK-400 and sediments at about 10.5 S. It has a covalent molecular weight on the order of 10(6). Proteinase K digestion produces VM-1 antibody reactive fragments, assumed to be polysaccharides, with a polydisperse molecular weight distribution in the range 5000 to 30,000. The VM-1 antigen is partially lost from solution on boiling and is no longer detectable in the aqueous or organic phase after chloroform-methanol extraction. The properties of the VM-1 antigen are consistent with those of a proteoglycan involved in attachment and spreading of keratinocytes and certain tumor cells on collagen.
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PMID:Inhibition of attachment and growth of tumor cells on collagen by a monoclonal antibody. 369 49

Although natural killer (NK) cell activity is remarkably stable in healthy individuals, the number and cytotoxicity of the cells fluctuate in disease. In man, regulatory mechanisms are virtually unexplored but depressed NK cell function accompanies most chronic diseases. A suppressive role of monocytes/macrophages has been reported. Since neutrophils (PMN) and monocytes (M) often respond reciprocally to pathologic stimuli, experiments were designed to investigate whether increments in PMN and M per se could influence NK cell function. Peripheral blood NK cells obtained by Percoll gradient centrifugation were either cocultured with various concentrations of autologous PMN or M or they were exposed to diffusates of these granulocytes in Millipore chambers. The treated NK cells were washed and then mixed with melanoma target cells in various effector:target cell ratios. It was observed that PMN diffusates augmented cytotoxicity whereas monocyte diffusates decreased the killing function of NK cells markedly and in a dose dependent fashion (P less than 0.001). The stimulatory effect of PMN diffusates was heat labile and not attributable to interferon. The inhibitory effect of M diffusates was heat stable, not due to prostaglandins or lysozyme, and irreversible within 6 hr of observation. Binding of effector to target cells was enhanced by PMN-media, and significantly inhibited by monocyte diffusates . It is therefore possible that factors elaborated by neutrophils and monocytes in vivo could also influence NK cell function.
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PMID:Modulation of natural killer (NK) cells by autologous neutrophils and monocytes. 620 25

Protamine sulfate reversibly inhibits serum-induced mitogenic stimulation of several nontransformed and neoplastic cell types in vitro. Fifty percent inhibition was induced by approximately 120-150 micrograms protamine sulfate/ml. Cells were affected directly, and inhibition depended on the duration of cell exposure. Heparin, chondroitin sulfate, heparan sulfate, and dextran sulfate neutralized protamine sulfate effects during the early stages of treatment. Nontransformed cells [bovine aortic endothelial cells, adult human gingival fibroblasts (strains 423 and 1101), fetal rat skin (strain 921-K) and muscle fibroblasts] required longer exposure to induce inhibition than did neoplastic cells [rat 3-methylcholanthrene-induced fibrosarcoma cell lines (MCA-6 and MCA-9), a macrophage-like cell line (NCTC-3749), Walker 256 rat carcinoma cells (ATCC-CCL-38), rat Morris hepatoma cells (ATCC-CCL-144), murine melanoma cells (B16), and rat bladder squamous cell carcinoma cells (804-G)]. Other polycationic compounds, including histone type VIII-S, poly-L-lysine, poly-L-arginine, and protamine (free base), were also effective inhibitors, whereas the basic proteins cytochrome c and lysozyme had no effect. Poly-L-histidine, poly-L-glutamic acid, poly-L-aspartic acid, and dextran blue also had no inhibitory effect.
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PMID:Protamine sulfate inhibition of serum-induced mitogenic responses: differential effects on normal and neoplastic cells. 621 Mar 90


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